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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Mdm2, transformed 3T3 cell double minute 2, p53 binding protein

MTBP, MDM2-binding protein
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Top mentioned proteins: mdm2, p53, CAN, TRF2, Ubiquitin
Papers on MTBP
MTBP Promotes the Invasion and Metastasis of Hepatocellular Carcinoma by Enhancing the MDM2-Mediated Degradation of E-Cadherin.
Li et al., Nanchang, China. In Dig Dis Sci, Dec 2015
BACKGROUND: Emerging evidence suggests that MTBP plays a role in cancer development and possibly progression, but its influence on hepatocellular carcinoma (HCC) remains unclear.
The quaternary structure of the eukaryotic DNA replication proteins Sld7 and Sld3.
Araki et al., Mishima, Japan. In Acta Crystallogr D Biol Crystallogr, Aug 2015
Recently, the Mdm2-binding protein was found to bind to treslin in humans, and its depletion causes defects in cells similar to the depletion of Sld7 in yeast, suggesting their functional relatedness and importance during the initiation step of DNA replication.
MTBP inhibits migration and metastasis of hepatocellular carcinoma.
Iwakuma et al., Beijing, China. In Clin Exp Metastasis, Apr 2015
MDM2 Binding Protein (MTBP) has been implicated in the suppression of cell migration and cancer metastasis.
MTBP is overexpressed in triple-negative breast cancer and contributes to its growth and survival.
Eischen et al., Nashville, United States. In Mol Cancer Res, 2014
MTBP (MDM2-binding protein), a gene linked to cellular proliferation and a transcriptional target of the MYC oncogene, is overexpressed in human malignancies, yet its contribution to cancer remains unresolved.
Oncogenic protein MTBP interacts with MYC to promote tumorigenesis.
Eischen et al., East Lansing, United States. In Cancer Res, 2014
Here we identify the MYC transcriptional cofactors TIP48 and TIP49 and MYC as novel binding partners of Mdm2-binding protein (MTBP), a functionally undefined protein that we show is oncogenic and overexpressed in many human cancers.
Identification of a heteromeric complex that promotes DNA replication origin firing in human cells.
Diffley et al., London, United Kingdom. In Science, 2013
We identified MDM two binding protein (MTBP) as a factor that interacts with Treslin/TICRR throughout the cell cycle.
MTBP suppresses cell migration and filopodia formation by inhibiting ACTN4.
Iwakuma et al., New Orleans, United States. In Oncogene, 2013
Murine double minute (MDM2) binding protein (MTBP) has been implicated in cancer progression.
MDM2 binding protein, a novel metastasis suppressor.
Agarwal et al., Kansas City, United States. In Cancer Metastasis Rev, 2012
MDM2 binding protein (MTBP) is a protein that interacts with oncoprotein murine double minute (MDM2), a major inhibitor of the tumor suppressor p53.
The enhancement of stability of p53 in MTBP induced p53-MDM2 regulatory network.
Singh et al., New Delhi, India. In Biosystems, 2012
We have modeled an MTBP-MDM2-p53 regulatory network by integrating p53-MDM2 autoregulatory model (Proctor and Gray, 2008) with the effect of a cellular protein MTBP (MDM2 binding protein) which is allowed to bind with MDM2 (Brady et al., 2005).
Loss of MTBP expression is associated with reduced survival in a biomarker-defined subset of patients with squamous cell carcinoma of the head and neck.
Boyd et al., Liverpool, United Kingdom. In Cancer, 2011
results represent the first examination of MTBP expression in human tissues and provide evidence for a p53 status-dependent role for MTBP in suppressing disease progression in squamous cell carcinoma of the head and neck patients
MTBP plays a crucial role in mitotic progression and chromosome segregation.
Iwakuma et al., New Orleans, United States. In Cell Death Differ, 2011
MTBP has an important role in recruiting and/or retaining the Mad1/Mad2 complex at the kinetochores during prometaphase, but its degradation is required for silencing the mitotic checkpoint.
A deficiency in Mdm2 binding protein inhibits Myc-induced B-cell proliferation and lymphomagenesis.
Eischen et al., Nashville, United States. In Oncogene, 2010
Mtbp functioned independent of Mdm2 and was a limiting factor for the proliferative and transforming functions of Myc. Thus, Mtbp is a previously unrecognized regulator of Myc-induced tumorigenesis.
Restoring p53 function in cancer: novel therapeutic approaches for applying the brakes to tumorigenesis.
Budillon et al., Napoli, Italy. In Recent Pat Anticancer Drug Discov, 2010
MDM2 is a p53 E3 ubiquitin ligase that mediates the ubiquitin-dependent degradation of p53 while p14/ARF is a small MDM2-binding protein that controls the activity of MDM2 by displacing p53 and preventing its degradation.
Solid-state and solution NMR studies of the CAP-Gly domain of mammalian dynactin and its interaction with microtubules.
Polenova et al., Newark, United States. In J Am Chem Soc, 2009
Despite the importance of the MT/MTBP assemblies, there remains virtually no structural or dynamic information about their interaction at the atomic level due to the inherent insolubility and lack of long-range order of MTs.
Mtbp haploinsufficiency in mice increases tumor metastasis.
Lozano et al., New Orleans, United States. In Oncogene, 2008
Mtbp haploinsufficiency in mice increases tumor metastasis
Regulation of p53 and MDM2 activity by MTBP.
Boyd et al., Liverpool, United Kingdom. In Mol Cell Biol, 2005
MTBP contributes to MDM2 activity and through this to negative regulation of p53
Structure-specific DNA-binding proteins as the foundation for three-dimensional chromatin organization.
Lobov et al., Saint Petersburg, Russia. In Int Rev Cytol, 2002
Telomere-binding TRF2/MTBP attaches telomeres to the nuclear envelope in interphase due to its rod-domain-like motif.
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